Solution structure of an SRYD-containing sequence (250?257) of the fibronectin-like Leishmania gp63 protein by restrained molecular dynamics
| Autor: | Vassilios Tsikaris, Maria Sakarellos-Daitsiotis, Manh Thong Cung, Piotr Orlewski, Constantinos Sakarellos, Ketty Soteriadou, Michel Marraud |
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| Rok vydání: | 1996 |
| Předmět: |
dmso solvent box
leishmania gp63 rgd Molecular model Tetrapeptide biology Stereochemistry Hydrogen bond Chemistry arginine ionic bridge Sequence (biology) cell-adhesion Biochemistry molecular dynamics Fibronectin Folding (chemistry) Molecular dynamics 2d nmr recognition site dimethyl-sulfoxide peptides biology.protein beta i-turn Two-dimensional nuclear magnetic resonance spectroscopy grgdsp |
| Zdroj: | Letters in Peptide Science. 3:317-326 |
| ISSN: | 1573-496X 0929-5666 |
| DOI: | 10.1007/bf00127666 |
| Popis: | The IASRYDQL synthetic octapeptide (250-257) of the Leishmania major surface glycoprotein gp63 efficiently inhibits parasite attachment to the macrophage receptors in in vitro experiments, and the SRYD-containing tetrapeptide mimics antigenically and functionally the RGDS sequence of fibronectin. The conformational properties of the octapeptide were investigated in dimethylsulfoxide (DMSO) with the combined use of NMR data (vicinal coupling constants, nuclear Overhauser effects (NOEs) and temperature coefficient values), molecular modeling by energy minimization and molecular dynamics. The structure is characterized by the high occurrence, exceeding 95%, of the Arg-Asp side-chain-side-chain ionic interaction, which plays a key role in the backbone folding through a distorted type-I beta-turn involving the Gln(256)-NH to Arg(253)-CO hydrogen bond. Letters in Peptide Science |
| Databáze: | OpenAIRE |
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